ID   A0A0F7JL96_9DEIO        Unreviewed;       395 AA.
AC   A0A0F7JL96;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=2-amino-3-ketobutyrate CoA ligase {ECO:0000313|EMBL:AKH17031.1};
GN   ORFNames=SY84_08130 {ECO:0000313|EMBL:AKH17031.1};
OS   Deinococcus soli (ex Cha et al. 2016).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=1309411 {ECO:0000313|EMBL:AKH17031.1, ECO:0000313|Proteomes:UP000034024};
RN   [1] {ECO:0000313|EMBL:AKH17031.1, ECO:0000313|Proteomes:UP000034024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N5 {ECO:0000313|EMBL:AKH17031.1,
RC   ECO:0000313|Proteomes:UP000034024};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Deinococcus soli/N5/whole genome sequencing.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU003693};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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DR   EMBL; CP011389; AKH17031.1; -; Genomic_DNA.
DR   RefSeq; WP_046843601.1; NZ_CP011389.1.
DR   AlphaFoldDB; A0A0F7JL96; -.
DR   KEGG; dch:SY84_08130; -.
DR   PATRIC; fig|1309411.5.peg.1661; -.
DR   OrthoDB; 9807157at2; -.
DR   Proteomes; UP000034024; Chromosome.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd06454; KBL_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR010962; AONS_Archaea/Firmicutes.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01825; gly_Cac_T_rel; 1.
DR   PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR   PANTHER; PTHR13693:SF3; LD36009P; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:AKH17031.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003693};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034024}.
FT   DOMAIN          42..383
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   395 AA;  42400 MW;  0920CFB4C4E0EFE1 CRC64;
     MATSLSDRLT AELSGLRESG LLIHPRVLDS ANRARTRVDG REVVNLASNN YLGFADHPAL
     KARAAEYLDR WGVGAGAVRT IAGTLRIHEE FEAQLAAFKH TGSALVLHSG FTTNQGVLGA
     LLREGDLVVS DELNHASIID GLRLTKATKK VFKHADPDDL ERLLKEHDTD GLKLVVTDGV
     FSMDGDVAPL DRLVAVARKY GAVTYVDDAH GSGVMGEAGR GTVHHFGFEY ADDVIQVGTL
     SKAWGGVGGY AAGHGDLRQL LINRARPYLF STAQAPATVG ALAAALDEVQ RDPTLMERLW
     ANTRYFKAEL QGLGFDIFGS TTPITPVIFG EAPAAFEASR LLFDRGVFAV GLGFPTVPRG
     LARIRNIVTA EHTRDDLDHA LQAYAEVGRA LGIIS
//